Conversion of Glycosylated Platycoside E to Deapiose-Xylosylated Platycodin D by Cytolase PCL5

Platycosides, the saponins abundant in Platycodi radix (the root of ), have diverse pharmacological activities and have been used as food supplements. Since deglycosylated saponins exhibit higher biological activity than glycosylated saponins, efforts are on to enzymatically convert glycosylated pla...

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Bibliographic Details
Published in:International journal of molecular sciences 2020-02, Vol.21 (4), p.1207
Main Authors: Shin, Kyung-Chul, Kim, Dae Wook, Woo, Hyun Sim, Oh, Deok-Kun, Kim, Yeong-Su
Format: Article
Language:English
Subjects:
cytolase
deapiosylation
dexylosylation
platycodon grandiflorum
platycoside
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Summary:Platycosides, the saponins abundant in Platycodi radix (the root of ), have diverse pharmacological activities and have been used as food supplements. Since deglycosylated saponins exhibit higher biological activity than glycosylated saponins, efforts are on to enzymatically convert glycosylated platycosides to deglycosylated platycosides; however, the lack of diversity and specificities of these enzymes has limited the kinds of platycosides that can be deglycosylated. In the present study, we examined the enzymatic conversion of platycosides and showed that Cytolase PCL5 completely converted platycoside E and polygalacin D3 into deapiose-xylosylated platycodin D and deapiose-xylosylated polygalacin D, respectively, which were identified by LC-MS analysis. The platycoside substrates were hydrolyzed through the following novel hydrolytic pathways: platycoside E → platycodin D3 → platycodin D → deapiosylated platycodin D → deapiose-xylosylated platycodin D; and polygalacin D3 → polygalacin D → deapiosylated polygalacin D → deapiose-xylosylated polygalacin D. Our results show that cytolast PCL5 may have a potential role in the development of biologically active platycosides that may be used for their diverse pharmacological activities.
ISSN:1422-0067
1422-0067
DOI:10.3390/ijms21041207